In this section
@article{Vydyanath:2012:10.1007/s10974-012-9286-9,
author = {Vydyanath, A and Gurnett, CA and Marston, S and Luther, PK},
doi = {10.1007/s10974-012-9286-9},
journal = {Journal of Muscle Research and Cell Motility},
pages = {61--74},
title = {Axial distribution of myosin binding protein-C is unaffected by mutations in human cardiac and skeletal muscle},
url = {http://dx.doi.org/10.1007/s10974-012-9286-9},
volume = {33},
year = {2012}
}
TY - JOUR
AB - Myosin binding protein-C (MyBP-C), a majorthick filament associated sarcomeric protein, plays animportant functional and structural role in regulating sarcomereassembly and crossbridge formation. Missing oraberrant MyBP-C proteins (both cardiac and skeletal) havebeen shown to cause both cardiac and skeletal myopathies,thereby emphasising its importance for the normal functioningof the sarcomere. Mutations in cardiac MyBP-C area major cause of hypertrophic cardiomyopathy (HCM),while mutations in skeletal MyBP-C have been implicatedin a disease of skeletal muscle—distal arthrogryposis type1 (DA-1). Here we report the first detailed electronmicroscopy studies on human cardiac and skeletal tissuescarrying MyBP-C gene mutations, using samples obtainedfrom HCM and DA-1 patients. We have used establishedimage averaging methods to identify and study the axialdistribution of MyBP-C on the thick filament by averagingprofile plots of the A-band of the sarcomere from electronmicrographs of human cardiac and skeletal myopathyspecimens. Due to the difficulty of obtaining normal humantissue, we compared the distribution to the A-band structurein normal frog skeletal, rat cardiac muscle and incardiac muscle of MyBP-C-deficient mice. Very similaroverall profile averages were obtained from the C-zones incardiac HCM samples and skeletal DA-1 samples withMyBP-C gene mutations, suggesting that mutations inMyBP-C do not
AU - Vydyanath,A
AU - Gurnett,CA
AU - Marston,S
AU - Luther,PK
DO - 10.1007/s10974-012-9286-9
EP - 74
PY - 2012///
SN - 1573-2657
SP - 61
TI - Axial distribution of myosin binding protein-C is unaffected by mutations in human cardiac and skeletal muscle
T2 - Journal of Muscle Research and Cell Motility
UR - http://dx.doi.org/10.1007/s10974-012-9286-9
UR - http://hdl.handle.net/10044/1/29931
VL - 33
ER -
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